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TitleReaction mechanism of hydroxynitrile lyases of the alpha/beta-hydrolase superfamily: the three-dimensional structure of the transient enzyme-substrate complex certifies the crucial role of LYS236
Journal, issue, pagesJ. Biol. Chem., Vol. 279, Page 20501-20510, Year 2004
Publish dateFeb 12, 2004 (structure data deposition date)
AuthorsGruber, K. / Gartler, G. / Krammer, B. / Schwab, H. / Kratky, C.
External linksJ. Biol. Chem. / PubMed:14998991
MethodsX-ray diffraction
Resolution1.7 - 2.9 Å
Structure data

PDB-1sc9:
Hydroxynitrile Lyase from Hevea brasiliensis in complex with the natural substrate acetone cyanohydrin
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1sci:
K236L mutant of hydroxynitrile lyase from Hevea brasiliensis
Method: X-RAY DIFFRACTION / Resolution: 2.18 Å

PDB-1sck:
K236L mutant of hydroxynitrile lyase from Hevea brasiliensis in complex with acetone
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1scq:
K236L mutant of hydroxynitrile lyase from Hevea brasiliensis in complex with acetonecyanohydrin
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-CNH:
2-HYDROXY-2-METHYLPROPANENITRILE

ChemComp-HOH:
WATER

ChemComp-ACN:
ACETONE

Source
  • hevea brasiliensis (rubber tree)
KeywordsLYASE / alpha-beta hydrolase fold / substrate complex / catalytic triad

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